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High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion

Academic Article
Publication Date:
2019
abstract:
The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2. However, the wild type G2 structure that have been used so far in comparative studies is bound to a crystallographic Cd, in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.
Iris type:
01.01 Articolo in rivista
Keywords:
AGel amyloidosis; Calcium; Gelsolin; Pathogenic mutations; X-ray crystallography
List of contributors:
Boni, Francesco; Scalone, Emanuele; Giorgino, Toni; Bollati, Michela; DE ROSA, Matteo; MILANI DE MAYO DE MARI, Mario; Mastrangelo, Eloise
Authors of the University:
BOLLATI MICHELA
BONI' FRANCESCO
DE ROSA MATTEO
GIORGINO TONI
MASTRANGELO ELOISE
MILANI DE MAYO DE MARI MARIO
Handle:
https://iris.cnr.it/handle/20.500.14243/365796
Published in:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (PRINT)
Journal
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http://www.scopus.com/record/display.url?eid=2-s2.0-85070378754&origin=inward
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